DPY30_CAEEL
ID DPY30_CAEEL Reviewed; 123 AA.
AC Q10661;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dosage compensation protein dpy-30;
DE AltName: Full=Protein dumpy-30;
GN Name=dpy-30; ORFNames=ZK863.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=7588066; DOI=10.1242/dev.121.10.3323;
RA Hsu D.R., Chuang P.-T., Meyer B.J.;
RT "DPY-30, a nuclear protein essential early in embryogenesis for
RT Caenorhabditis elegans dosage compensation.";
RL Development 121:3323-3334(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=8939869; DOI=10.1126/science.274.5293.1732;
RA Lieb J.D., Capowski E.E., Meneely P., Meyer B.J.;
RT "DPY-26, a link between dosage compensation and meiotic chromosome
RT segregation in the nematode.";
RL Science 274:1732-1736(1996).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23884442; DOI=10.1242/dev.094292;
RA Webster C.M., Wu L., Douglas D., Soukas A.A.;
RT "A non-canonical role for the C. elegans dosage compensation complex in
RT growth and metabolic regulation downstream of TOR complex 2.";
RL Development 140:3601-3612(2013).
RN [5]
RP FUNCTION, INTERACTION WITH JMJD-3.1, AND DISRUPTION PHENOTYPE.
RX PubMed=25124442; DOI=10.1126/science.1255885;
RA Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
RA Jarriault S.;
RT "Sequential histone-modifying activities determine the robustness of
RT transdifferentiation.";
RL Science 345:826-829(2014).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN THE SET2 COMPLEX, INTERACTION WITH CFP-1 AND WDR-5.1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=31602465; DOI=10.1093/nar/gkz880;
RA Beurton F., Stempor P., Caron M., Appert A., Dong Y., Chen R.A., Cluet D.,
RA Coute Y., Herbette M., Huang N., Polveche H., Spichty M., Bedet C.,
RA Ahringer J., Palladino F.;
RT "Physical and functional interaction between SET1/COMPASS complex component
RT CFP-1 and a Sin3S HDAC complex in C. elegans.";
RL Nucleic Acids Res. 47:11164-11180(2019).
CC -!- FUNCTION: Essential for dosage compensation (PubMed:7588066). Required
CC for the sex-specific association of the dosage compensation complex
CC proteins dpy-27 and dpy-26 with the hermaphrodite X chromosomes
CC (PubMed:7588066, PubMed:8939869). Plays a role in developmental rate
CC and body fat regulation downstream of the TOR complex 2
CC (PubMed:23884442). Required for the robust transdifferentiation of the
CC Y rectal cell to the PDA motor neuron during larval development
CC (PubMed:25124442). {ECO:0000269|PubMed:23884442,
CC ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:7588066,
CC ECO:0000269|PubMed:8939869}.
CC -!- SUBUNIT: Component of the SET2 complex (also known as the SET1/COMPASS
CC complex), which contains at least set-2, swd-2.1, cfp-1, rbbp-5, wdr-
CC 5.1, dpy-30 and ash-2 (PubMed:31602465). Within the complex, interacts
CC with cfp-1 and wdr-5.1 (PubMed:31602465). Interacts with jmjd-3.1
CC (PubMed:25124442). {ECO:0000269|PubMed:25124442,
CC ECO:0000269|PubMed:31602465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7588066}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in all
CC stages. {ECO:0000269|PubMed:7588066}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown suppresses the growth
CC delay and elevated body fat index of the TOR complex 2 mutant rict-1
CC (PubMed:23884442). Results in disruption of the invariant
CC transdifferentiation of the Y rectal cell to the PDA motor neuron
CC (PubMed:25124442). {ECO:0000269|PubMed:23884442,
CC ECO:0000269|PubMed:25124442}.
CC -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR EMBL; U21302; AAA92286.1; -; Genomic_DNA.
DR EMBL; Z78019; CAB01452.1; -; Genomic_DNA.
DR PIR; T28060; T28060.
DR RefSeq; NP_506058.1; NM_073657.4.
DR AlphaFoldDB; Q10661; -.
DR SMR; Q10661; -.
DR BioGRID; 44694; 16.
DR DIP; DIP-27173N; -.
DR IntAct; Q10661; 7.
DR STRING; 6239.ZK863.6.3; -.
DR EPD; Q10661; -.
DR PaxDb; Q10661; -.
DR PeptideAtlas; Q10661; -.
DR EnsemblMetazoa; ZK863.6.1; ZK863.6.1; WBGene00001088.
DR EnsemblMetazoa; ZK863.6.2; ZK863.6.2; WBGene00001088.
DR GeneID; 179671; -.
DR KEGG; cel:CELE_ZK863.6; -.
DR UCSC; ZK863.6.1; c. elegans.
DR CTD; 179671; -.
DR WormBase; ZK863.6; CE15445; WBGene00001088; dpy-30.
DR eggNOG; KOG4109; Eukaryota.
DR GeneTree; ENSGT01030000238170; -.
DR HOGENOM; CLU_135823_2_0_1; -.
DR InParanoid; Q10661; -.
DR OMA; KHSNGCD; -.
DR OrthoDB; 1602399at2759; -.
DR PhylomeDB; Q10661; -.
DR Reactome; R-CEL-3214841; PKMTs methylate histone lysines.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR PRO; PR:Q10661; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001088; Expressed in embryo and 3 other tissues.
DR GO; GO:0044666; C:MLL3/4 complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IMP:WormBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR037856; Sdc1/DPY30.
DR PANTHER; PTHR23356; PTHR23356; 1.
DR Pfam; PF05186; Dpy-30; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome.
FT CHAIN 1..123
FT /note="Dosage compensation protein dpy-30"
FT /id="PRO_0000114682"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 12837 MW; D54E5AD91CD53929 CRC64;
MADQTASAEV ATEKMDTAEA PAAAPAASAA APAEAESNEN TTVPSNVLSA NGGQQTGNQS
APRNTSTVPT RQYLDSTVVP ILLQGLGALA KDRPENPIEF LANFLLREKD RYNAENQNPA
GQQ
